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Database: UniProt
Entry: Q2NTA8
LinkDB: Q2NTA8
Original site: Q2NTA8 
ID   ALR_SODGM               Reviewed;         356 AA.
AC   Q2NTA8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   16-JAN-2019, entry version 80.
DE   RecName: Full=Alanine racemase {ECO:0000255|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000255|HAMAP-Rule:MF_01201};
GN   Name=alr; OrderedLocusNames=SG1342;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K.,
RA   Hattori M., Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights
RT   into the symbiotic lifestyle of Sodalis glossinidius in the tsetse
RT   host.";
RL   Genome Res. 16:149-156(2006).
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC         ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01201};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01201}.
DR   EMBL; AP008232; BAE74617.1; -; Genomic_DNA.
DR   RefSeq; WP_011411170.1; NC_007712.1.
DR   ProteinModelPortal; Q2NTA8; -.
DR   SMR; Q2NTA8; -.
DR   STRING; 343509.SG1342; -.
DR   PRIDE; Q2NTA8; -.
DR   EnsemblBacteria; BAE74617; BAE74617; SG1342.
DR   KEGG; sgl:SG1342; -.
DR   eggNOG; ENOG4105CJ4; Bacteria.
DR   eggNOG; COG0787; LUCA.
DR   HOGENOM; HOG000076274; -.
DR   KO; K01775; -.
DR   OMA; RDLELCS; -.
DR   OrthoDB; 859043at2; -.
DR   BioCyc; SGLO343509:SGP1_RS11800-MONOMER; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001932; Chromosome.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01201; Ala_racemase; 1.
DR   InterPro; IPR000821; Ala_racemase.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR011079; Ala_racemase_C.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   Pfam; PF00842; Ala_racemase_C; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PRINTS; PR00992; ALARACEMASE.
DR   SMART; SM01005; Ala_racemase_C; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Isomerase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN         1    356       Alanine racemase.
FT                                /FTId=PRO_1000066039.
FT   ACT_SITE     35     35       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    253    253       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   BINDING     130    130       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01201}.
FT   BINDING     301    301       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
FT   MOD_RES      35     35       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01201}.
SQ   SEQUENCE   356 AA;  38378 MW;  3484A08AAB98067E CRC64;
     MPRPIVAKVD SAVLASNLSI VRRHAPQAQV WSVVKANGYG HGLNTVWQGL QQTDGFALLD
     LHEAVVLREK GWRGPILLLE GFFQPADLAV IDRYRLTTVV HSDWQIEALR RMTPRAPLDI
     YLKLNSGMNR LGFSERALPG AWQSLNALKH VATLTLMSHF AYADMPEGVE GQMAVVARAG
     EGLTGPRCLA NSAATLWHPA THGQWVRPGI ILYGASPSGN WQDIAASGLR PVMTLQSELI
     AVQSVPAGGR IGYGGRHRVS ETHRVGVVAC GYADGYPRHA PTGTPILVDG VRTSTLGAVS
     MDMLMVDLQL CPKARIGSAV ELWGDHVKID EVAASAGTLG YELMSALAPR VTVQIR
//
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